PDBsum entry 4b7e

Oxidoreductase/peptide

PDB id: 4b7e

Contents

Protein chains

349 a.a.

17 a.a.

Ligands

OGA

SO4 ×5

GOL ×4

Metals

_ZN

Waters ×165

PDB id:

4b7e

Name:

Oxidoreductase/peptide

Title:

Factor inhibiting hif-1 alpha in complex with consensus ankyrin repeat domain-leu peptide (20-mer)

Structure:

Hypoxia-inducible factor 1-alpha inhibitor. Chain: a. Synonym: factor inhibiting hif, factor inhibiting hif-1, fih-1, hypoxia-inducible factor asparagine hydroxylase. Engineered: yes. Consensus ankyrin repeat domain-leu. Chain: b. Engineered: yes. Other_details: synthetic peptide (20-mer)

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Synthetic construct. Organism_taxid: 32630

Resolution:

2.50Å R-factor: 0.226 R-free: 0.255

Authors:

R.Chowdhury,W.Ge,C.J.Schofield

Key ref:

M.Yang et al. (2013). Substrate selectivity analyses of factor inhibiting hypoxia-inducible factor. Angew Chem Int Ed Engl, 52, 1700-1704. PubMed id: 23296631

Date:

17-Aug-12 Release date: 23-Jan-13

Protein chain

Q9NWT6  (HIF1N_HUMAN) -  Hypoxia-inducible factor 1-alpha inhibitor from Homo sapiens

Seq: 349 a.a.

Struc: 349 a.a.

Protein chain

No UniProt id for this chain

Struc: 17 a.a.

Enzyme reactions

• Enzyme class 2: Chain A: E.C.1.14.11.30 - hypoxia-inducible factor-asparagine dioxygenase.
• Reaction: L-asparaginyl-[hypoxia-inducible factor alpha subunit] + 2-oxoglutarate + O2 = (3S)-3-hydroxy-L-asparaginyl-[hypoxia-inducible factor alpha subunit] + succinate + CO2
• Cofactor: Fe(2+); L-ascorbate

Fe(2+) L-ascorbate (Bound ligand (Het Group name = GOL) matches with 50.00% similarity)

• Enzyme class 3: Chain A: E.C.1.14.11.n4 - ?????

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

Angew Chem Int Ed Engl 52:1700-1704 (2013)

PubMed id: 23296631

Substrate selectivity analyses of factor inhibiting hypoxia-inducible factor.

M.Yang, A.P.Hardy, R.Chowdhury, N.D.Loik, J.S.Scotti, J.S.McCullagh, T.D.Claridge, M.A.McDonough, W.Ge, C.J.Schofield.

ABSTRACT

Substrate specificity: Biochemical and crystallographic analyses reveal the hypoxia-inducible factor hydroxylase (FIH) as being promiscuous with respect to the residues that it can hydroxylate in β-position, which in addition to Asn, Asp, and His include Leu and Ser residues. The Ser substrate is oxidized to an epimeric β-geminal diol product.